› 5ml1

Solution NMR

NMR Structure of the Littorina littorea metallothionein, a snail MT folding into three distinct domains

Released:
DOI: 10.2210/pdb5ml1/pdb
PDB entry 5ml1 coloured by chain, ensemble of 20 models, front view.
PDB entry 5ml1 coloured by chain, ensemble of 20 models, side view.
PDB entry 5ml1 coloured by chain, ensemble of 20 models, top view.
Source organism: Littorina littorea
Primary publication:
Structural Adaptation of a Protein to Increased Metal Stress: NMR Structure of a Marine Snail Metallothionein with an Additional Domain.
Baumann C, Beil A, Jurt S, Niederwanger M, Palacios O, Capdevila M, Atrian S, Dallinger R, Zerbe O
Angew Chem Int Ed Engl 56 4617-4622 (2017)
PMID: 28332759

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188298 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative metallothionein Chain: A
Molecule details ›
Chain: A
Length: 102 amino acids
Theoretical weight: 10.2 KDa
Source organism: Littorina littorea
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q962G0 (Residues: 1-100; Coverage: 100%)

Ligands and Environments

1 bound ligand:
Ligand CD 9 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 84%
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Trace metals in oysters: molecular and cellular mechanisms and ecotoxicological impacts.
Wang et al. (2018)
15 other articles

1 mention without citation

Evolution of Cd2+ and Cu+ binding in Helix pomatia metallothioneins.
Valsecchi et al. (2023)